Structural requirements of glycosaminoglycans for facilitating amyloid fibril formation of human serum amyloid A

Amyloid ◽  
2016 ◽  
Vol 23 (2) ◽  
pp. 67-75 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Aki Yamamoto ◽  
Shiori Watanabe ◽  
Sanae Takahashi ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Structural Requirements ◽  
Amyloid A ◽  
Amyloid Fibril Formation

Effect of lipid environment on amyloid fibril formation of human serum amyloid A

2017 ◽  
Vol 202 ◽  
pp. 6-12 ◽  
Author(s):  
Masafumi Tanaka ◽  
Ayaka Nishimura ◽  
Haruka Takeshita ◽  
Hiroka Takase ◽  
Toshiyuki Yamada ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Amyloid Fibril Formation ◽  
Lipid Environment

Acceleration of amyloid fibril formation by carboxyl-terminal truncation of human serum amyloid A

2018 ◽  
Vol 639 ◽  
pp. 9-15 ◽  
Author(s):  
Masafumi Tanaka ◽  
Toru Kawakami ◽  
Nozomi Okino ◽  
Kaoru Sasaki ◽  
Kiwako Nakanishi ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Amyloid Fibril Formation ◽  
Carboxyl Terminal

scholarly journals Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner

2018 ◽  
Vol 54 (28) ◽  
pp. 3532-3535 ◽  
Author(s):  
Shobini Jayaraman ◽  
Donald L. Gantz ◽  
Christian Haupt ◽  
Marcus Fändrich ◽  
Olga Gursky
Keyword(s):  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Dependent Manner ◽  
Amyloid A ◽  
Amyloid Fibril Formation

Serum amyloid A can solubilize diverse phospholipids and their hydrolytic products to form lipoprotein nanoparticles, which hampers amyloid fibril formation.

Fibril formation from recombinant human serum amyloid A

1994 ◽  
Vol 1226 (3) ◽  
pp. 323-329 ◽  
Author(s):  
Toshiyuki Yamada ◽  
Barbara Kluve-Beckerman ◽  
Juris J. Liepnieks ◽  
Merrill D. Benson
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals The potential role of glycosaminoglycans in serum amyloid A fibril formation by in silico approaches

2021 ◽  
pp. 100080
Author(s):  
Martyna Maszota-Zieleniak ◽  
Annemarie Danielsson ◽  
Sergey A. Samsonov
Keyword(s):  
In Silico ◽  
Serum Amyloid A ◽  
Potential Role ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Amyloid A

Genetic Isofocusing Variant of Human Serum Amyloid A

1991 ◽  
pp. 20-23
Author(s):  
A. Steinmetz ◽  
H. Vitt ◽  
S. Motzny ◽  
H. Kaffarnik
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

1989 ◽  
Vol 263 (2) ◽  
pp. 365-370 ◽  
Author(s):  
A F Strachan ◽  
E G Shephard ◽  
D U Bellstedt ◽  
G A Coetzee ◽  
D R van der Westhuyzen ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Gel Filtration ◽  
Density Lipoprotein ◽  
High Titre ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Buffer Solutions ◽  
Wide Range ◽  
Serum Amyloid A Protein

Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (greater than 90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at greater than 7 M-urea. By immunizing with apo-SAA adsorbed to acid-treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.

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